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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

Akap10  -  A kinase (PRKA) anchor protein 10

Mus musculus

Synonyms: 1500031L16Rik, A-kinase anchor protein 10, mitochondrial, AKAP-10, B130049N18Rik, D-AKAP-2, ...
 
 
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High impact information on Akap10

  • D-AKAP2 from all three species is highly enriched in mitochondria [1].
  • Full-length D-AKAP2 from various tissues shows different molecular weights, possibly because of alternative splicing or posttranslational modifications [1].
  • Therefore, D-AKAP2 represents a novel family of proteins. cDNA cloning from a mouse testis library identified the full length D-AKAP2 [2].
  • The presence of this domain raises the intriguing possibility that D-AKAP2 may interact with a Galpha protein thus providing a link between the signaling machinery at the plasma membrane and the downstream kinase [2].
  • The second folded region contained a highly protected PKA binding site and a more solvent-accessible PDZ binding motif, which may serve as a potential targeting domain for D-AKAP2 [3].
 

Biological context of Akap10

  • DXMS has verified the multi-domain architecture of D-AKAP2 implied by sequence homology and has provided unique insight into the accessibility of the PKA binding site [3].
  • To understand the molecular basis for this "dual" functionality, we have examined the pH-dependence, the salt-dependence, and the kinetics of binding of the A-kinase binding (AKB) domain of D-AKAP2 to the regulatory subunit isoforms of PKA [4].
 

Anatomical context of Akap10

 

Physical interactions of Akap10

  • In pull-down experiments, D-AKAP2 tightly bound PDZK1 as well as N+/H+ exchanger regulator factor (NHERF-1), but the latter with an apparent fourfold lower affinity [5].
  • Hydrogen/deuterium (H/D) exchange combined with mass spectrometry (DXMS) was used to probe backbone structural changes of an alpha-helical A-kinase binding (AKB) motif from D-AKAP2 docked to both RIalpha and RIIalpha D/D domains [6].
 

Other interactions of Akap10

  • CONCLUSION: We conclude that D-AKAP2 anchors protein kinase A (PKA) to PDZK1 and to a lesser extent to NHERF-1 [5].
  • Since PDZK1 and NHERF-1 both sequester NaPi-IIa to the apical membrane, D-AKAP2 may play an important role in the parathyroid hormone (PTH)-mediated regulation of NaPi-IIa by compartmentalization of PKA [5].
 

Analytical, diagnostic and therapeutic context of Akap10

References

  1. Cloning and mitochondrial localization of full-length D-AKAP2, a protein kinase A anchoring protein. Wang, L., Sunahara, R.K., Krumins, A., Perkins, G., Crochiere, M.L., Mackey, M., Bell, S., Ellisman, M.H., Taylor, S.S. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  2. D-AKAP2, a novel protein kinase A anchoring protein with a putative RGS domain. Huang, L.J., Durick, K., Weiner, J.A., Chun, J., Taylor, S.S. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  3. Domain organization of D-AKAP2 revealed by enhanced deuterium exchange-mass spectrometry (DXMS). Hamuro, Y., Burns, L., Canaves, J., Hoffman, R., Taylor, S., Woods, V. J. Mol. Biol. (2002) [Pubmed]
  4. Isoform specific differences in binding of a dual-specificity A-kinase anchoring protein to type I and type II regulatory subunits of PKA. Burns, L.L., Canaves, J.M., Pennypacker, J.K., Blumenthal, D.K., Taylor, S.S. Biochemistry (2003) [Pubmed]
  5. PDZK1: II. an anchoring site for the PKA-binding protein D-AKAP2 in renal proximal tubular cells. Gisler, S.M., Madjdpour, C., Bacic, D., Pribanic, S., Taylor, S.S., Biber, J., Murer, H. Kidney Int. (2003) [Pubmed]
  6. Distinct interaction modes of an AKAP bound to two regulatory subunit isoforms of protein kinase A revealed by amide hydrogen/deuterium exchange. Burns-Hamuro, L.L., Hamuro, Y., Kim, J.S., Sigala, P., Fayos, R., Stranz, D.D., Jennings, P.A., Taylor, S.S., Woods, V.L. Protein Sci. (2005) [Pubmed]
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